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Magnesium in PDB 2ein: Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State

Enzymatic activity of Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State

All present enzymatic activity of Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State:
1.9.3.1;

Protein crystallography data

The structure of Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State, PDB code: 2ein was solved by K.Muramoto, K.Hirata, K.Shinzawa-Itoh, S.Yoko-O, E.Yamashita, H.Aoyama, T.Tsukihara, S.Yoshikawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 187.810, 203.581, 177.927, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 25.8

Other elements in 2ein:

The structure of Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State also contains other interesting chemical elements:

Zinc (Zn) 14 atoms
Iron (Fe) 4 atoms
Copper (Cu) 6 atoms
Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State (pdb code 2ein). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State, PDB code: 2ein:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2ein

Go back to Magnesium Binding Sites List in 2ein
Magnesium binding site 1 out of 2 in the Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg518

b:35.4
occ:1.00
OD1 A:ASP369 2.1 31.3 1.0
OE1 B:GLU198 2.1 37.2 1.0
NE2 A:HIS368 2.2 26.8 1.0
O B:HOH2032 2.4 63.6 1.0
O A:HOH2031 2.4 26.2 1.0
O B:HOH2033 2.4 43.9 1.0
CE1 A:HIS368 3.1 30.1 1.0
CD B:GLU198 3.1 46.8 1.0
CG A:ASP369 3.3 36.9 1.0
CD2 A:HIS368 3.4 30.3 1.0
O A:HOH2035 3.4 49.7 1.0
OE2 B:GLU198 3.5 45.5 1.0
O A:HOH2010 3.9 21.4 1.0
OD2 A:ASP369 4.1 26.9 1.0
O B:SER197 4.2 41.2 1.0
CB A:ASP369 4.3 36.2 1.0
O A:HOH2020 4.3 32.2 1.0
O A:HOH2038 4.3 24.1 1.0
ND1 A:HIS368 4.3 36.5 1.0
CG A:HIS368 4.5 29.2 1.0
OD2 B:ASP173 4.5 59.4 1.0
CG B:GLU198 4.5 44.2 1.0
O A:HOH2023 4.8 33.3 1.0
CB B:GLU198 4.8 31.7 1.0
OG1 A:THR294 4.9 38.2 1.0

Magnesium binding site 2 out of 2 in 2ein

Go back to Magnesium Binding Sites List in 2ein
Magnesium binding site 2 out of 2 in the Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Zinc Ion Binding Structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Mg1518

b:48.1
occ:1.00
OE1 O:GLU198 2.1 52.8 1.0
OD1 N:ASP369 2.1 49.3 1.0
NE2 N:HIS368 2.3 52.7 1.0
O O:HOH3033 2.4 48.8 1.0
O O:HOH3032 2.4 61.2 1.0
O N:HOH3031 2.4 42.9 1.0
CE1 N:HIS368 2.9 46.4 1.0
CG N:ASP369 3.3 49.6 1.0
CD O:GLU198 3.3 59.6 1.0
O N:HOH3035 3.3 42.2 1.0
CD2 N:HIS368 3.5 47.4 1.0
OE2 O:GLU198 3.8 60.4 1.0
O N:HOH3010 3.9 41.3 1.0
OD2 N:ASP369 4.1 46.7 1.0
ND1 N:HIS368 4.1 45.5 1.0
CB N:ASP369 4.1 41.5 1.0
O O:SER197 4.2 46.3 1.0
O N:HOH3020 4.3 54.8 1.0
O N:HOH3038 4.4 29.7 1.0
CG N:HIS368 4.4 41.2 1.0
OD2 O:ASP173 4.5 54.4 1.0
CG O:GLU198 4.5 56.7 1.0
O N:HOH3023 4.6 43.7 1.0
OG1 N:THR294 4.8 40.2 1.0
CB O:GLU198 4.9 49.2 1.0

Reference:

K.Muramoto, K.Hirata, K.Shinzawa-Itoh, S.Yoko-O, E.Yamashita, H.Aoyama, T.Tsukihara, S.Yoshikawa. A Histidine Residue Acting As A Controlling Site For Dioxygen Reduction and Proton Pumping By Cytochrome C Oxidase Proc.Natl.Acad.Sci.Usa V. 104 7881 2007.
ISSN: ISSN 0027-8424
PubMed: 17470809
DOI: 10.1073/PNAS.0610031104
Page generated: Sun Aug 10 10:39:05 2025

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